Cellular Process of Polystyrene Nanoparticles Entry into Wheat Roots.

Nanoscale plastic particles are widely found in the terrestrial environment and being increasingly studied in recent years. However, the knowledge of their translocation and accumulation mechanism controlled by nanoplastic characterizations in plant tissues is limited, especially in plant cells. Here, 20 mg L-1 polystyrene nanoparticles (PS NPs) with different sizes and amino/carboxy groups were employed to investigate the internalization process in wheat roots and cells. From the results, we found that the uptake of small-size PS NPs in the root tissues was increased compared to that of large-size ones, but no PS NPs were observed in the vascular cylinder. Similar results were observed in their cellular uptake process. Besides, the cell wall could block the entry of large-size PS NPs while the cell membrane could not. The -NH2 group on the PS NPs surface could benefit their tissular/cellular translocation compared to the -COOH group. The internalization of PS NPs was controlled by both particle size and surface functional group, and the size should be the primary factor. Our findings offer important information for understanding the PS NPs behaviors in plant tissues, especially at the cellular level, and assessing their potential risk to food safety, quality, and agricultural sustainability.

Indole-3-acetic acid enhances the co-transport of proton and phenanthrene mediated by TaSAUR80-5A in wheat roots.

Polycyclic aromatic hydrocarbons (PAHs) are a type of organic pollution that can accumulate in crops and hazard human health. This study used phenanthrene (PHE) as a model PAH and employed hydroponic experiments to illustrate the role of indole-3-acetic acid (IAA) in the regulation of PHE accumulation in wheat roots. At optimal concentrations, wheat roots treated with PHE + IAA showed a 46.9% increase in PHE concentration, whereas treatment with PHE + P-chlorophenoxyisobutyric acid resulted in a 38.77% reduction. Transcriptome analysis identified TaSAUR80-5A as the crucial gene for IAA-enhancing PHE uptake. IAA increases plasma membrane H+-ATPase activity, promoting active transport of PHE via the PHE/H+ cotransport mechanism. These results provide not only the theoretical basis necessary to better understand the function of IAA in PAHs uptake and transport by staple crops, but also a strategy for controlling PAHs accumulation in staple crops and enhancing phytoremediation of PAH-contaminated environments.

Mechanistic insights into auxin-enhancing polycyclic aromatic hydrocarbon uptake by wheat roots: Evidence from in situ intracellular pH and root-surface H+ flux.

Polycyclic aromatic hydrocarbons (PAHs) are a group of extremely carcinogenic organic pollutants. Our previous findings have demonstrated that plant roots actively take up PAHs through co-transport with H+ ions. Auxin serves as a pivotal regulator of plant growth and development. However, it remains unclear whether the hormone can enhance the uptake of PAHs by plant roots. Hence, the wheat root exposed to PAHs with/without auxins was set to investigate how the auxin promotes the PAHs uptake by roots. In our study, auxin could significantly enhance the uptake of PAHs after 4 h of exposure. After the addition of auxin, the root tissue cytoplasmic pH value was decreased and the H+ influx was observed, indicating that the extracellular space was alkalinized in a short time. The increased H+ influx rate enhanced the uptake of PAHs. In addition, the H+-ATPase activity was also increased, suggesting that auxin activated two distinct and antagonistic H+ flux pathways, and the H+ influx pathway was dominant. Our findings offer important information for exploring the mechanism underlying auxin regulation of PAHs uptake and the phytoremediation of PAH-contaminated soil and water.

New mechanistic insights into PAHs transport across wheat root cell membrane: Evidence for ABC transporter mediation.

Polycyclic aromatic hydrocarbons (PAHs) are a class of highly carcinogenic organic pollutants. Our previous results revealed that the active uptake of PAHs by plant roots is performed through H+/PAHs co-transport. However, the proteins and mechanisms of co-transport of PAHs remain unknown. We hypothesized that ABC transporters are involved in PAHs co-transport via the roots. We found a total of 47 ABC transporters with alkalinity and hydrophobicity which were up-regulated or newly expressed in the wheat roots after phenanthrene exposure. And the concentration of ABC transporters rose. There was a positive relationship between the concentration of phenanthrene and ABC transporter expression in the wheat roots. Additionally, the trend observed in the ABC transporters expression was also found in the gene expression. With energies below -6 kcal mol-1, a stable docking conformation formed between ABC transporters and PAHs. π-π stacking and van der Waals force bound PAHs to ABCB or ABCG. The binding strength of ABCB subfamily proteins with homodimers is stronger than that of ABCG subfamily proteins with single molecules. ABC transporters may transport PAHs by forming a dimer-shaped pocket, translocating it into cells, then opening it within the cells, to release the bound PAHs. These results contributed to our understanding of how ABC transporters aid plant root uptake of PAHs.

Mechanistic insights into phenanthrene acropetal translocation via wheat xylem: Separation and identification of transfer proteins.

Polycyclic aromatic hydrocarbons (PAHs) have the potential to cause cancer, teratogenicity, and mutagenesis in humans. Long-term plant safe production relies on how PAHs are transported and coordinated across organs. However, the acropetal transfer mechanism of PAHs in staple crop stems, particularly in xylem, a critical path, is unknown. Herein, we first confirmed the presence of specific interaction between the proteins and phenanthrene by employing the magnetic phenanthrene-bound bead immunoassay and label free liquid chromatograph mass spectrometer (LC-MS/MS), suggesting that peroxidase (uniprot accession: A0A3B5XXD0) and unidentified proteins (uniprot accession: A0A3B6LUC6) may function as the carriers to load and acropetally translocate phenanthrene (a model PAH) in wheat xylem. This specified binding of protein-phenanthrene may form through hydrophobic interactions in the conservative binding region, as revealed by protein structural investigations and molecular docking. To further investigate the role of these proteins in phenanthrene solubilization, phenanthrene exposure was conducted: a substantial quantity of peroxidase was produced; an unusually high expression of uncharacterized proteins was observed, indicating their positive effects in the acropetal transfer of phenanthrene in wheat xylem. These data confirmed that the two proteins are crucial in the solubilization of phenanthrene in wheat xylem sap. Our findings provide fresh light on the molecular mechanism of PAH loading in plant xylem and techniques for ensuring the security of staple crops and improving the efficacy of phytoremediation in a PAH-contaminated environment.